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- W1992633719 abstract "Complimentary pulsed EPR techniques (ESEEM, ENDOR, HYSCORE), over multiple frequencies (X, Ka, Q-bands), were used to characterize bonding interactions of the [2Fe-2S] redox active center of the Outer Mitochondrial Membrane protein, MitoNEET. MitoNEET is the first example of a 3Cys-1His coordinated [2Fe-2S] cluster containing protein. Specifically targeting the uniquely single Fe-histidine interaction, EPR investigations integrated both natural abundance 14N and isotopically labeled 15N protein to determine the hyperfine tensor of a strongly coupled imidazole nitrogen of the bound histidine ligand. 1D-ESEEM experiments in the 31, 35GHz frequency region resulted in deep modulation patterns indicative of being near the “exact cancellation” limit and was favorable for a more direct spectral assignment of nuclear quadrupolar transition frequencies. Assignment of His87 as the bound ligand was supported by parallel experiments using H87C mutant. An additional advantage of these higher field experiments allows for greater resolved g-anisotropy and a finer degree of orientation-selected experiments, in progress. These should provide a more accurate description of the [2Fe-2S] ligand bonding interaction important for understanding the electronic structure of this new class of redox active proteins." @default.
- W1992633719 created "2016-06-24" @default.
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- W1992633719 date "2009-02-01" @default.
- W1992633719 modified "2023-10-05" @default.
- W1992633719 title "Multifrequency Pulsed EPR investigation of Fe-histidine Interaction of the Uniquely Coordinated [2Fe-2S] Cluster in the Outer Mitochondrial Membrane Protein, MitoNEET" @default.
- W1992633719 doi "https://doi.org/10.1016/j.bpj.2008.12.1541" @default.
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